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==REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM==
==REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM==
<StructureSection load='1fmf' size='340' side='right'caption='[[1fmf]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
<StructureSection load='1fmf' size='340' side='right'caption='[[1fmf]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"clostridium_tetanomorphum"_bulloch_et_al._1919 "clostridium tetanomorphum" bulloch et al. 1919]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMF FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1be1|1be1]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylaspartate_mutase Methylaspartate mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.1 5.4.99.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmf OCA], [https://pdbe.org/1fmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmf RCSB], [https://www.ebi.ac.uk/pdbsum/1fmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmf ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmf OCA], [https://pdbe.org/1fmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmf RCSB], [https://www.ebi.ac.uk/pdbsum/1fmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GMSS_CLOTT GMSS_CLOTT]] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526]<ref>PMID:8051138</ref>
[https://www.uniprot.org/uniprot/GMSS_CLOTT GMSS_CLOTT] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526]<ref>PMID:8051138</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fmf ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fmf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Uniformly (13)C,(15)N-labeled MutS, the coenzyme B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum, was prepared by overexpression from an Escherichia coli strain. Multidimensional heteronuclear NMR spectroscopic experiments with aqueous solutions of (13)C,(15)N-labeled MutS provided signal assignments for roughly 90% of the 1025 hydrogen, 651 carbon, and 173 nitrogen atoms and resulted in about 1800 experimental restraints. Based on the information from the NMR experiments, the structure of MutS was calculated, confirming the earlier, less detailed structure obtained with (15)N-labeled MutS. The refined analysis allowed a precise determination of the secondary and tertiary structure including several crucial side chain interactions. The structures of (the apoprotein) MutS in solution and of the B(12)-binding subunit in the crystal of the corresponding homologous holoenzyme from Clostridium cochlearium differ only in a section that forms the well-structured helix alpha1 in the crystal structure and that also comprises the cobalt-coordinating histidine residue. In the apoprotein MutS, this part of the B(12)-binding subunit is dynamic. The carboxy-terminal end of this section is conformationally flexible and has significant propensity for an alpha-helical structure ("nascent helix"). This dynamic section in MutS is a decisive element for the binding of the nucleotide moiety of coenzyme B(12) and appears to be stabilized as a helix (alpha1) upon trapping of the nucleotide of the B(12) cofactor.
A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum.,Hoffmann B, Tollinger M, Konrat R, Huhta M, Marsh EN, Krautler B Chembiochem. 2001 Sep 3;2(9):643-55. PMID:11828501<ref>PMID:11828501</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fmf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium tetanomorphum bulloch et al. 1919]]
[[Category: Clostridium tetanomorphum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Methylaspartate mutase]]
[[Category: Hoffmann B]]
[[Category: Hoffmann, B]]
[[Category: Huhta M]]
[[Category: Huhta, M]]
[[Category: Konrat R]]
[[Category: Konrat, R]]
[[Category: Kraeutler B]]
[[Category: Kraeutler, B]]
[[Category: Marsh ENG]]
[[Category: Marsh, E N.G]]
[[Category: Tollinger M]]
[[Category: Tollinger, M]]
[[Category: Isomerase]]
[[Category: Nucleotide binding fold]]
[[Category: Rossmann fold]]
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